In recent years, it has become apparent that an Nε-acetylation of the lysine residue in N-terminal region of a core histone plays an important role in the control of gene expression of eukaryotes. The enzyme of a histone acetyltransferase responsible for the acetylation and the enzyme of a histone deacetylase responsible for deacetylation were cloned in 1996 for the first time, and after that, a plurality of molecules having similar activities have been found. In recent years, furthermore, beside histone, it has been found that various kinds of non-histone proteins such as p53, TCF, and HMG-1 could be acetylated. It has been pointed out that the acetylation may be post-translation modification that plays various roles as equally as phosphorylation.
To search for an unknown novel acetylation protein as described above, there is no need to discuss the usefulness of a probe molecule that recognizes an Nε-acetyllysine residue specifically and irrespectively of the adjacent amino acid. An antibody has been considered as the most suitable molecule for the object. However, the antibody capable of recognizing acetyllysine under various conditions irrespective of the types of the adjacent amino acids has been hardly reported.